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Conserved domains on  [gi|15596259|ref|NP_249753|]
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hypothetical protein PA1062 [Pseudomonas aeruginosa PAO1]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11441181)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

CATH:  3.40.630.30
EC:  2.3.-.-
Gene Ontology:  GO:0016746|GO:0008080
PubMed:  27367672|26818562|15581578|10940244
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-154 3.67e-19

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 79.27  E-value: 3.67e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596259   3 RLRAAETGDIEAMTDLL---LRHGPNPWNHLP--EEGVRAHLRAIADGEVRAVLAERDDRLLGFASFRrtedfahyqPQR 77
Cdd:COG1247   3 TIRPATPEDAPAIAAIYneaIAEGTATFETEPpsEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLG---------PFR 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596259  78 ADAPRAYICEA--VVHPAAAGQGLGSALLEAVLAQLADEGIEDVYIDRHEENLASAGMMRKAGFVELETYADPARRPNG 154
Cdd:COG1247  74 PRPAYRGTAEEsiYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGR 152
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-154 3.67e-19

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 79.27  E-value: 3.67e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596259   3 RLRAAETGDIEAMTDLL---LRHGPNPWNHLP--EEGVRAHLRAIADGEVRAVLAERDDRLLGFASFRrtedfahyqPQR 77
Cdd:COG1247   3 TIRPATPEDAPAIAAIYneaIAEGTATFETEPpsEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLG---------PFR 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596259  78 ADAPRAYICEA--VVHPAAAGQGLGSALLEAVLAQLADEGIEDVYIDRHEENLASAGMMRKAGFVELETYADPARRPNG 154
Cdd:COG1247  74 PRPAYRGTAEEsiYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGR 152
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 12-139 5.76e-15

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 67.16  E-value: 5.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596259    12 IEAMTDLLLRHGPNPWnhlPEEGVRAHLRAIADGEVRAVLAERDDRLLGFASFRrtedfahyqPQRADAPRAYICEAVVH 91
Cdd:pfam00583   1 LEALYELLSEEFPEPW---PDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLS---------IIDDEPPVGEIEGLAVA 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 15596259    92 PAAAGQGLGSALLEAVLAQLADEGIEDVYIDRHEENLASAGMMRKAGF 139
Cdd:pfam00583  69 PEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 50-122 1.06e-08

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 49.20  E-value: 1.06e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596259  50 VLAERDDRLLGFASFRRTEDFAHYqpqradaprAYICEAVVHPAAAGQGLGSALLEAVLAQLADEGIEDVYID 122
Cdd:cd04301   2 LVAEDDGEIVGFASLSPDGSGGDT---------AYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 50-153 1.35e-05

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 42.70  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596259    50 VLAERDDRLLGFASFRRTEDFAHyqpqradaprayICEAVVHPAAAGQGLGSALLEAVLAQLADEGIEDVYIDRHEENLA 129
Cdd:TIGR01575  34 LLARIGGKVVGYAGVQIVLDEAH------------ILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIA 101

                          90       100
                  ....*....|....*....|....
gi 15596259   130 SAGMMRKAGFveletyADPARRPN 153
Cdd:TIGR01575 102 AQALYKKLGF------NEIAIRRN 119
PRK07757 PRK07757
N-acetyltransferase;
1-119 6.55e-05

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 40.95  E-value: 6.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596259    1 MHRLRAAETGDIEAMTDLLlrhgpnpwNHLPEEGV---RA------HLRAIadgevraVLAERDDRLLGFASFR-RTEDF 70
Cdd:PRK07757   1 MMEIRKARLSDVKAIHALI--------NVYAKKGLmlpRSldelyeNIRDF-------YVAEEEGEIVGCCALHiLWEDL 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 15596259   71 AHyqpqradaprayICEAVVHPAAAGQGLGSALLEAVLAQLADEGIEDV 119
Cdd:PRK07757  66 AE------------IRSLAVSEDYRGQGIGRMLVEACLEEARELGVKRV 102
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-154 3.67e-19

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 79.27  E-value: 3.67e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596259   3 RLRAAETGDIEAMTDLL---LRHGPNPWNHLP--EEGVRAHLRAIADGEVRAVLAERDDRLLGFASFRrtedfahyqPQR 77
Cdd:COG1247   3 TIRPATPEDAPAIAAIYneaIAEGTATFETEPpsEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLG---------PFR 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596259  78 ADAPRAYICEA--VVHPAAAGQGLGSALLEAVLAQLADEGIEDVYIDRHEENLASAGMMRKAGFVELETYADPARRPNG 154
Cdd:COG1247  74 PRPAYRGTAEEsiYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGR 152
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 12-139 5.76e-15

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 67.16  E-value: 5.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596259    12 IEAMTDLLLRHGPNPWnhlPEEGVRAHLRAIADGEVRAVLAERDDRLLGFASFRrtedfahyqPQRADAPRAYICEAVVH 91
Cdd:pfam00583   1 LEALYELLSEEFPEPW---PDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLS---------IIDDEPPVGEIEGLAVA 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 15596259    92 PAAAGQGLGSALLEAVLAQLADEGIEDVYIDRHEENLASAGMMRKAGF 139
Cdd:pfam00583  69 PEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 3-157 1.38e-12

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 61.55  E-value: 1.38e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596259   3 RLRAAETGDIEAMTDLLLRHgpnpwnhlpeegvrahlrAIADGEVRAVLAERDDRLLGFASFRRTedfahyqpqraDAPR 82
Cdd:COG1246   2 TIRPATPDDVPAILELIRPY------------------ALEEEIGEFWVAEEDGEIVGCAALHPL-----------DEDL 52

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596259  83 AYICEAVVHPAAAGQGLGSALLEAVLAQLADEGIEDVYIdrhEENLASAGMMRKAGFVELETYADPARRPNGSGR 157
Cdd:COG1246  53 AELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFL---LTTSAAIHFYEKLGFEEIDKEDLPYAKVWQRDS 124
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
4-149 1.80e-11

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 58.56  E-value: 1.80e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596259   4 LRAAETGDIEAMTDLLLRhgpnPWNHLPEEGVRAHLRAIADGEvRAVLAERDDRLLGFASFRRTEDfahyqpqRADAPRA 83
Cdd:COG3153   1 IRPATPEDAEAIAALLRA----AFGPGREAELVDRLREDPAAG-LSLVAEDDGEIVGHVALSPVDI-------DGEGPAL 68

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596259  84 YICEAVVHPAAAGQGLGSALLEAVLAQLADEGIEDVYIDRHEENLAsagMMRKAGFVELETYADPA 149
Cdd:COG3153  69 LLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLP---FYERFGFRPAGELGLTL 131
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 3-163 6.48e-11

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 57.70  E-value: 6.48e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596259   3 RLRAAETGDIEAMTDLLLRHG---PNPWNHLPEEGVRAHLRAIADGEVR------AVLAERDDRLLGFASFRRTEDFAHY 73
Cdd:COG1670   9 RLRPLRPEDAEALAELLNDPEvarYLPGPPYSLEEARAWLERLLADWADggalpfAIEDKEDGELIGVVGLYDIDRANRS 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596259  74 qpqradaprayiCEA--VVHPAAAGQGLGSALLEAVLAQLADE-GIEDVYIDRHEENLASAGMMRKAGFVElETYADPAR 150
Cdd:COG1670  89 ------------AEIgyWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGFRL-EGTLRDAL 155

                       170
                ....*....|...
gi 15596259 151 RPNGSGRSTVCHR 163
Cdd:COG1670 156 VIDGRYRDHVLYS 168
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 70-144 1.57e-10

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 55.05  E-value: 1.57e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596259  70 FAHYQPQRADaPRAYICEAVVHPAAAGQGLGSALLEAVLAQLADEGIEDVYIDRHEENLASAGMMRKAGFVELET 144
Cdd:COG0456   2 FALLGLVDGG-DEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGE 75
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 30-150 4.57e-10

N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 54.67  E-value: 4.57e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596259  30 LPEEGVRAHLRAIADGEVRA--VLAERDDRLLGFASFRRTEDfahyqpqradaPRAYICEAVVHPAAAGQGLGSALLEAV 107
Cdd:COG0454  15 LLIEALDAELKAMEGSLAGAefIAVDDKGEPIGFAGLRRLDD-----------KVLELKRLYVLPEYRGKGIGKALLEAL 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15596259 108 LAQLADEGIEDVYIDRHEENLASAGMMRKAGFVELETYADPAR 150
Cdd:COG0454  84 LEWARERGCTALELDTLDGNPAAIRFYERLGFKEIERYVAYVG 126
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 50-122 1.06e-08

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 49.20  E-value: 1.06e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596259  50 VLAERDDRLLGFASFRRTEDFAHYqpqradaprAYICEAVVHPAAAGQGLGSALLEAVLAQLADEGIEDVYID 122
Cdd:cd04301   2 LVAEDDGEIVGFASLSPDGSGGDT---------AYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 3-140 5.63e-07

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 46.57  E-value: 5.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596259     3 RLRAAETGDIEAMTDLL----LRHGPNPWnHLPEEGVRAHLRAIADGEVRA-----VLAERDDRLLGFASFRRTEDFAHy 73
Cdd:pfam13302   3 LLRPLTEEDAEALFELLsdpeVMRYGVPW-PLTLEEAREWLARIWAADEAErgygwAIELKDTGFIGSIGLYDIDGEPE- 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596259    74 qpqraDAPRAYIceavVHPAAAGQGLGSALLEAVLAQLADE-GIEDVYIDRHEENLASAGMMRKAGFV 140
Cdd:pfam13302  81 -----RAELGYW----LGPDYWGKGYATEAVRALLEYAFEElGLPRLVARIDPENTASRRVLEKLGFK 139
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
11-149 2.30e-06

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 45.29  E-value: 2.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596259  11 DIEAMTDLLLRHGPnpWNHLPEEGVRAHLRAIADGevravlaerDDRLLGFASFRrtedfaHYqpqRADAPR------AY 84
Cdd:COG3981  38 DFEAWLERLLDEEK--GEELPEGWVPATTYWLVDE---------DGRIVGAINLR------HE---LNEFLLrvgghiGY 97

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596259  85 IceavVHPAAAGQGLGSALLEAVLAQLADEGIEDVYIDRHEENLASAGMMRKAGFVELETYADPA 149
Cdd:COG3981  98 G----VRPSERGKGYATEMLRLALEEARELGLDRVLITCDKDNIASRKVIEANGGVLEDEVVDEE 158
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
90-146 4.56e-06

Predicted acetyltransferase, GNAT family [General function prediction only];


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 42.97  E-value: 4.56e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15596259  90 VHPAAAGQGLGSALLEAVLAQLADEGIEDVYIDRHEENLASAGMMRKAGFVELETYA 146
Cdd:COG3393  23 THPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEYA 79
COG3818 COG3818
Predicted N-acetyltransferase, GNAT superfamily [General function prediction only];
4-141 6.10e-06

Predicted N-acetyltransferase, GNAT superfamily [General function prediction only];


Pssm-ID: 443030 [Multi-domain]  Cd Length: 168  Bit Score: 44.16  E-value: 6.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596259   4 LRAAETGDIEAMTDLLLRHGPNPwNHLPEEGVRaHLRAIADgevRAVLAERDDRLLGFA-SFRRTEDFA--HYQPQRADA 80
Cdd:COG3818   7 IRDAREHDLDAVLALNNAAVPAV-SPLDAARLA-RLHEQAA---YARVAEVDGEVAGFLlAFGPGADYDspNYRWFAERY 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596259  81 PR-AYICEAVVHPAAAGQGLGSALLEAVLAQLADEGIE----DVYIDRHeeNLASAGMMRKAGFVE 141
Cdd:COG3818  82 DNfLYIDRIVVAPSARGRGLGRALYADVFSYARARGVPrvtcEVNLEPP--NPGSLAFHARLGFRE 145
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 40-121 7.30e-06

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 43.41  E-value: 7.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596259    40 RAIADGEVRAVLAERDDRLLGFASFRRtedfahyqpqradapRAYICEAVVHPAAAGQGLGSALLEAVLAQLADEGIEDV 119
Cdd:pfam13673  24 ERIDQGEYFFFVAFEGGQIVGVIALRD---------------RGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLS 88


                  ..
gi 15596259   120 YI 121
Cdd:pfam13673  89 EL 90
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 50-141 7.85e-06

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 42.06  E-value: 7.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596259    50 VLAERDDRLLGFASFRRTEDFAHYQpqradapRAYICeavVHPAAAGQGLGSALLEAVLAQLADEGIEDVYIDRHEENla 129
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLDDEGALA-------ELRLA---VHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRA-- 73

                          90
                  ....*....|..
gi 15596259   130 sAGMMRKAGFVE 141
Cdd:pfam13508  74 -AAFYEKLGFEE 84
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 50-153 1.35e-05

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 42.70  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596259    50 VLAERDDRLLGFASFRRTEDFAHyqpqradaprayICEAVVHPAAAGQGLGSALLEAVLAQLADEGIEDVYIDRHEENLA 129
Cdd:TIGR01575  34 LLARIGGKVVGYAGVQIVLDEAH------------ILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIA 101

                          90       100
                  ....*....|....*....|....
gi 15596259   130 SAGMMRKAGFveletyADPARRPN 153
Cdd:TIGR01575 102 AQALYKKLGF------NEIAIRRN 119
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
44-122 1.97e-05

Predicted N-acyltransferase, GNAT family [General function prediction only];


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 42.09  E-value: 1.97e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596259  44 DGEVRAVLAERDDRLLGFASFRRTEDfahyqpqradaPRAYICEAVVHPAAAGQGLGSALLEAVLAQLADEGIEDVYID 122
Cdd:COG2153  31 DEDARHLLAYDDGELVATARLLPPGD-----------GEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLS 98
PRK07757 PRK07757
N-acetyltransferase;
1-119 6.55e-05

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 40.95  E-value: 6.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596259    1 MHRLRAAETGDIEAMTDLLlrhgpnpwNHLPEEGV---RA------HLRAIadgevraVLAERDDRLLGFASFR-RTEDF 70
Cdd:PRK07757   1 MMEIRKARLSDVKAIHALI--------NVYAKKGLmlpRSldelyeNIRDF-------YVAEEEGEIVGCCALHiLWEDL 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 15596259   71 AHyqpqradaprayICEAVVHPAAAGQGLGSALLEAVLAQLADEGIEDV 119
Cdd:PRK07757  66 AE------------IRSLAVSEDYRGQGIGRMLVEACLEEARELGVKRV 102
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 90-141 5.72e-04

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 38.37  E-value: 5.72e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15596259   90 VHPAAAGQGLGSALLEAVLAQLADEGIEDVYIDRHEENLASAGMMRKAGFVE 141
Cdd:PRK09491  71 VDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNE 122
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
 48-126 2.31e-03

GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both CoA and acetyl-CoA. They are characterized by highly conserved glycine, a cysteine residue in the acetyl-CoA binding site near the acetyl group, their small size compared with other GNATs and a lack of of an obvious substrate-binding site. It is proposed that they transfer an acetyl group from acetyl-CoA to one or more unidentified aliphatic amines via an acetyl (cysteine) enzyme intermediate. The substrate might be another macromolecule.


Pssm-ID: 434030 [Multi-domain]  Cd Length: 79  Bit Score: 35.19  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596259    48 RAVLAERDDRLLGFASFRRTEDfahyqpqradapRAYICEAVVHPAAAGQGLGSALLEAVLAQLADEGIEDV-------- 119
Cdd:pfam14542   1 RFEIRVDGGAEVAFLTYRRGDG------------VLIITHTEVPPALRGQGIASKLVKAALDDAREEGLKIVplcsyvaa 68


                  ....*..
gi 15596259   120 YIDRHEE 126
Cdd:pfam14542  69 YLEKHPE 75
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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